Hysteretic Behavior of Proprotein Convertase 1/3 (PC1/3)

• Autor(a) principal: Icimoto, Marcelo Y. [UNIFESP]
• Data de Publicação: 2011
• Outros Autores: Barros, Nilana M., Ferreira, Juliana C. [UNIFESP], Marcondes, Marcelo F. [UNIFESP], Andrade, Douglas [UNIFESP], Machado, Mauricio F. [UNIFESP], Juliano, Maria A. [UNIFESP], Judice, Wagner A., Juliano, Luiz [UNIFESP], Oliveira, Vitor [UNIFESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• dARK ID: ark:/48912/0013000003n1v
• Texto Completo: http://dx.doi.org/10.1371/journal.pone.0024545; http://repositorio.unifesp.br/handle/11600/34049

The proprotein convertases (PCs) are calcium-dependent proteases responsible for processing precursor proteins into their active forms in eukariotes. the PC1/3 is a pivotal enzyme of this family that participates in the proteolytic maturation of prohormones and neuropeptides inside the regulated secretory pathway. in this paper we demonstrate that mouse proprotein convertase 1/3 (mPC1/3) has a lag phase of activation by substrates that can be interpreted as a hysteretic behavior of the enzyme for their hydrolysis. This is an unprecedented observation in peptidases, but is frequent in regulatory enzymes with physiological relevance. the lag phase of mPC1/3 is dependent on substrate, calcium concentration and pH. This hysteretic behavior may have implications in the physiological processes in which PC1/3 participates and could be considered an additional control step in the peptide hormone maturation processes as for instance in the transformation of proinsulin to insulin.